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Robert J. Lefkowitz

Researcher at Howard Hughes Medical Institute

Publications -  867
Citations -  153371

Robert J. Lefkowitz is an academic researcher from Howard Hughes Medical Institute. The author has contributed to research in topics: Receptor & G protein-coupled receptor. The author has an hindex of 214, co-authored 860 publications receiving 147995 citations. Previous affiliations of Robert J. Lefkowitz include University of Nice Sophia Antipolis & University of Stuttgart.

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Substitution of an extracellular cysteine in the β2-adrenergic receptor enhances agonist-promoted phosphorylation and receptor desensitization

TL;DR: Not only is impaired desensitization associated with decreased phosphorylation associated withIncreased agonist promoted receptor phosphorylated, but enhanced desensItization is accompanied by increased agonists promoted receptorosphorylation in intact cells.
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Marked enhancement in myocardial function resulting from overexpression of a human β–adrenergic receptor gene

TL;DR: Transgenic mice with intense cardiac expression of a human beta-adrenergic receptor gene were engineered and shown to display marked improvements in baseline myocardial and left ventricular function, suggesting a novel approach for increasing myocardIAL function with important clinical implications.
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Solubilization of rat liver alpha 1-adrenergic receptors. Agonist specific alteration in receptor binding affinity.

TL;DR: An improved method for the solubilization of the alpha 1-adrenergic receptors in rat liver, utilizing digitonin, glycerol and sonication, is described, consistent with the notion that these receptors might be capable of existing in two distinct conformational states with the high affinity state for agonists being favored by solubILization.
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Synthesis of iodine-125 labeled (+/-)-15-(4-azidobenzyl)carazolol: a potent beta-adrenergic photoaffinity probe.

TL;DR: The compounds described have been shown to be potent beta-adrenergic antagonists by virtue of their ability to inhibit beta-Adrenergic stimulation of adenylate cyclase or to compete for the binding of another beta-ADrenergic ligand, [125I]cyanopindolol, to the beta- adrenergic receptors of frog erythrocytes.